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Database: UniProt
Entry: A0A1J9PG44_9EURO
LinkDB: A0A1J9PG44_9EURO
Original site: A0A1J9PG44_9EURO 
ID   A0A1J9PG44_9EURO        Unreviewed;      1004 AA.
AC   A0A1J9PG44;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   27-MAR-2024, entry version 28.
DE   RecName: Full=DNA mismatch repair protein MSH3 {ECO:0000256|ARBA:ARBA00019000};
DE   AltName: Full=DNA mismatch repair protein msh3 {ECO:0000256|ARBA:ARBA00022151};
GN   ORFNames=AJ78_04821 {ECO:0000313|EMBL:OJD14874.1};
OS   Emergomyces pasteurianus Ep9510.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Ajellomycetaceae; Emergomyces.
OX   NCBI_TaxID=1447872 {ECO:0000313|EMBL:OJD14874.1, ECO:0000313|Proteomes:UP000182235};
RN   [1] {ECO:0000313|EMBL:OJD14874.1, ECO:0000313|Proteomes:UP000182235}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UAMH 9510 {ECO:0000313|EMBL:OJD14874.1,
RC   ECO:0000313|Proteomes:UP000182235};
RG   The Broad Institute Genomics Platform;
RA   Cuomo C.A., Munoz J.F., Imamovic A., Priest M.E., Young S., Clay O.K.,
RA   McEwen J.G.;
RT   "Emmonsia species relationships and genome sequence.";
RL   Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Component of the post-replicative DNA mismatch repair system
CC       (MMR). Heterodimerizes with MSH2 to form MutS beta, which binds to DNA
CC       mismatches thereby initiating DNA repair. MSH3 provides substrate-
CC       binding and substrate specificity to the complex. When bound, the MutS
CC       beta heterodimer bends the DNA helix and shields approximately 20 base
CC       pairs. Acts mainly to repair insertion-deletion loops (IDLs) from 2 to
CC       13 nucleotides in size, but can also repair base-base and single
CC       insertion-deletion mismatches that occur during replication. After
CC       mismatch binding, forms a ternary complex with the MutL alpha
CC       heterodimer, which is thought to be responsible for directing the
CC       downstream MMR events, including strand discrimination, excision, and
CC       resynthesis. ATP binding and hydrolysis play a pivotal role in mismatch
CC       repair functions. {ECO:0000256|ARBA:ARBA00025373}.
CC   -!- SUBUNIT: Heterodimer consisting of MSH2-MSH3 (MutS beta). Forms a
CC       ternary complex with MutL alpha (MLH1-PMS1).
CC       {ECO:0000256|ARBA:ARBA00025902}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC   -!- SIMILARITY: Belongs to the DNA mismatch repair MutS family.
CC       {ECO:0000256|ARBA:ARBA00006271}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:OJD14874.1}.
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DR   EMBL; LGRN01000191; OJD14874.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1J9PG44; -.
DR   STRING; 1447872.A0A1J9PG44; -.
DR   OrthoDB; 168255at2759; -.
DR   Proteomes; UP000182235; Unassembled WGS sequence.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0140664; F:ATP-dependent DNA damage sensor activity; IEA:InterPro.
DR   GO; GO:0030983; F:mismatched DNA binding; IEA:InterPro.
DR   GO; GO:0006298; P:mismatch repair; IEA:InterPro.
DR   Gene3D; 1.10.1420.10; -; 3.
DR   Gene3D; 3.40.1170.10; DNA repair protein MutS, domain I; 1.
DR   Gene3D; 3.30.420.110; MutS, connector domain; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   InterPro; IPR007695; DNA_mismatch_repair_MutS-lik_N.
DR   InterPro; IPR017261; DNA_mismatch_repair_MutS/MSH.
DR   InterPro; IPR000432; DNA_mismatch_repair_MutS_C.
DR   InterPro; IPR007696; DNA_mismatch_repair_MutS_core.
DR   InterPro; IPR016151; DNA_mismatch_repair_MutS_N.
DR   InterPro; IPR036187; DNA_mismatch_repair_MutS_sf.
DR   InterPro; IPR007860; DNA_mmatch_repair_MutS_con_dom.
DR   InterPro; IPR036678; MutS_con_dom_sf.
DR   InterPro; IPR045076; MutS_family.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   PANTHER; PTHR11361:SF34; DNA MISMATCH REPAIR PROTEIN MSH1, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR11361; DNA MISMATCH REPAIR PROTEIN MUTS FAMILY MEMBER; 1.
DR   Pfam; PF01624; MutS_I; 1.
DR   Pfam; PF05188; MutS_II; 1.
DR   Pfam; PF05192; MutS_III; 1.
DR   Pfam; PF00488; MutS_V; 1.
DR   PIRSF; PIRSF037677; DNA_mis_repair_Msh6; 1.
DR   SMART; SM00534; MUTSac; 1.
DR   SMART; SM00533; MUTSd; 1.
DR   SUPFAM; SSF55271; DNA repair protein MutS, domain I; 1.
DR   SUPFAM; SSF53150; DNA repair protein MutS, domain II; 1.
DR   SUPFAM; SSF48334; DNA repair protein MutS, domain III; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   PROSITE; PS00486; DNA_MISMATCH_REPAIR_2; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   DNA damage {ECO:0000256|ARBA:ARBA00022763};
KW   DNA repair {ECO:0000256|ARBA:ARBA00023204};
KW   DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000182235}.
FT   DOMAIN          872..888
FT                   /note="DNA mismatch repair proteins mutS family"
FT                   /evidence="ECO:0000259|PROSITE:PS00486"
FT   REGION          569..599
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          603..637
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        576..590
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1004 AA;  111754 MW;  E55A47DB711C03B0 CRC64;
     MTFYLTCGRQ LRRPVLSFCS HCFAVRNACR TPFLAPLGVP LQFNRGAKRK STAKLKDLPQ
     GRLEPIEPYS PLVNDAPQYP TVIQGARNNM QKFKNCVLLT RVGNFYELYF EQAEEYAALL
     NLKLAQKKTN AGAVPMAGFP FFQLDRFLKI LVQDLNKYVA ISEEFANNVV GKAKSGGLQF
     DRKVARIVTP GTLIDEKFMD PYENNFLLSV YMATTRSEET GILSPEQHSS ISSSQPIGLS
     WLDLSTGDFF TQRTTAQMLP SAVARIGARE IVIDENLGVK FRQELQAIVG QDQQHLLTSF
     KCPSDMRTLS DWASIFETSI SPEVASMFTT EETAACNILL EYVQVQTQGV KMKLQAPRRR
     HLDDSMTIDR NSLRGLEILE TARDGLGKGS LLHAVRRTST KSGARLLKDR LTSPSTSLHV
     ISERLNLVSK FREDEDLRQN IILLLKRSFD AQRLVQKFSL GRGDPDDLIC LSKAIQASQE
     IKSVLLRNID QYWELSDDQR SDEQANHDVT CSLRSMVGRL NFDGPETLSQ RILAAIDEEG
     LLQKQRIEDD AAAEAAALAQ EVILNEGSSE DLEAMPKTVK GQRGKQKESN GAEQGDGNTW
     IMRRDASKNL QKLHDALDLL KAEKAELTEK LRDTAGTDNL SLKWTPGLGH IVHMKGVKAS
     QQSIEALGAT RTVSSSKSTR SFYLSSWSQL GARLENARFH ILSEEQRIFE ELRQAVILNL
     VKLRRNAAVL DELDVACSFA SLAEEQQMVR PVVNNSKSHK IVGGRHPTVK LGLEEQGRPF
     VSNDCFIGEQ ERIWLITGPN MGGKSTFLRQ NALITILAQV GSFVPAEHAE IGVVDQIFSR
     IGAADDLFRD QSTFMVEMLE TATILKSATS RSFVIMDEVG RGTTPEDGTA VGFACLHHLH
     NVNQCRTLFA THFHVLADMT ARFERLGRYC TDVKEDSSGA FSFVHRLRRG VNRESHALKV
     ARLAGLPESA IDVAKDVLRK ISDCGSFEGK EPASAPTKVT RSIS
//
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